Choose your preferred view mode

Please select whether you prefer to view the MDPI pages with a view tailored for mobile displays or to view the MDPI
pages in the normal scrollable desktop version. This selection will be stored into your cookies and used automatically
in next visits. You can also change the view style at any point from the main header when using the pages with your
mobile device.

Abstract

Adenovirus (AdV) capsid organization is considerably complex, not only because of its large size (~950 Å) and triangulation number (pseudo T = 25), but also because it contains four types of minor proteins in specialized locations modulating the quasi-equivalent icosahedral interactions. Up until 2009, only its major components (hexon, penton, and fiber) had separately been described in atomic detail. Their relationships within the virion, and the location of minor coat proteins, were inferred from combining the known crystal structures with increasingly more detailed cryo-electron microscopy (cryoEM) maps. There was no structural information on assembly intermediates. Later on that year, two reports described the structural differences between the mature and immature adenoviral particle, starting to shed light on the different stages of viral assembly, and giving further insights into the roles of core and minor coat proteins during morphogenesis [1,2]. Finally, in 2010, two papers describing the atomic resolution structure of the complete virion appeared [3,4]. These reports represent a veritable tour de force for two structural biology techniques: X-ray crystallography and cryoEM, as this is the largest macromolecular complex solved at high resolution by either of them. In particular, the cryoEM analysis provided an unprecedented clear picture of the complex protein networks shaping the icosahedral shell. Here I review these latest developments in the field of AdV structural studies.
View Full-Text

Supplementary material

It has come to my attention that my article "Latest Insights on Adenovirus Structure and Assembly" (Viruses 2012, 4, 847-877) [1] contains an inaccurate statement.
On page 864, the caption for Figure 7 reads: "There are four potential cleavage sites in pTP but they have not been experimentally verified". However, three of these sites have been experimentally confirmed in vitro using recombinant AVP and pTP, as described in Webster A, Leith I.R., Hay R.T.: Activation of adenovirus-coded protease and processing of preterminal protein. J. Virol. 1994, 68, 7292-7300 [2].